Header list of 1wsx.pdb file
Complete list - r 2 2 Bytes
HEADER APOPTOSIS 12-NOV-04 1WSX
TITLE SOLUTION STRUCTURE OF MCL-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYELOID CELL LEUKEMIA SEQUENCE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 152-308;
COMPND 5 SYNONYM: MYELOID CELL LEUKEMIA-1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: MCL-1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX6P-3;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PLASMID
KEYWDS HELICAL BUNDLE, APOPTOSIS, BCL-2, BH3, MCL-1
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.L.DAY,L.CHEN,S.J.RICHARDSON,P.J.HARRISON,D.C.HUANG,M.G.HINDS
REVDAT 4 02-MAR-22 1WSX 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1WSX 1 VERSN
REVDAT 2 08-MAR-05 1WSX 1 JRNL
REVDAT 1 23-NOV-04 1WSX 0
JRNL AUTH C.L.DAY,L.CHEN,S.J.RICHARDSON,P.J.HARRISON,D.C.HUANG,
JRNL AUTH 2 M.G.HINDS
JRNL TITL SOLUTION STRUCTURE OF PROSURVIVAL MCL-1 AND CHARACTERIZATION
JRNL TITL 2 OF ITS BINDING BY PROAPOPTOTIC BH3-ONLY LIGANDS
JRNL REF J.BIOL.CHEM. V. 280 4738 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15550399
JRNL DOI 10.1074/JBC.M411434200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, XPLOR-NIH 2
REMARK 3 AUTHORS : BRUKER AG (XWINNMR),
REMARK 3 C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 3974 CONSTAINTS, 3507 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 335
REMARK 3 DIHEDRAL ANGLE RESTRAINTS AND 66 HYDROGEN BOND CONSTRAINTS
REMARK 4
REMARK 4 1WSX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000023962.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM U-15N MCL-1; 1MM U-13C,15N
REMARK 210 MCL-1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNHA; 3D_15N-SEPARATED_NOESY;
REMARK 210 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AV
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, DISTANCE
REMARK 210 GEOMETRY, SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 256
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY, STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLAR NMR TECHNIQUES.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 GLU A 152 -149.74 -71.02
REMARK 500 1 GLU A 182 -44.58 -141.04
REMARK 500 1 GLU A 206 -35.95 -34.09
REMARK 500 1 ASP A 217 84.67 -170.62
REMARK 500 1 PHE A 235 39.70 -97.66
REMARK 500 1 ARG A 291 24.33 41.15
REMARK 500 1 TRP A 293 -63.51 -29.00
REMARK 500 1 GLN A 303 -69.62 -102.09
REMARK 500 2 GLU A 152 -153.50 -90.06
REMARK 500 2 LYS A 175 -124.61 -72.22
REMARK 500 2 LEU A 180 173.14 -59.97
REMARK 500 2 GLU A 182 -50.07 -150.04
REMARK 500 2 GLU A 206 -35.77 -34.53
REMARK 500 2 ASP A 217 72.11 -166.70
REMARK 500 2 LYS A 236 -79.15 -26.23
REMARK 500 2 ASP A 237 -70.13 -172.92
REMARK 500 2 ASN A 263 60.23 65.35
REMARK 500 2 ARG A 291 23.51 43.88
REMARK 500 3 ASP A 153 52.94 -107.84
REMARK 500 3 PRO A 179 157.25 -48.19
REMARK 500 3 GLU A 206 -35.09 -34.07
REMARK 500 3 ASP A 217 79.56 -168.76
REMARK 500 3 PHE A 235 39.46 -92.94
REMARK 500 3 ARG A 291 23.91 43.92
REMARK 500 3 HIS A 301 30.68 -87.86
REMARK 500 4 GLU A 206 -35.06 -34.14
REMARK 500 4 ASP A 217 76.95 -162.97
REMARK 500 4 PHE A 235 39.72 -98.56
REMARK 500 4 ASN A 263 54.21 70.36
REMARK 500 4 ARG A 291 24.13 45.01
REMARK 500 4 PHE A 300 50.66 -115.68
REMARK 500 5 ASP A 153 71.75 -117.82
REMARK 500 5 LEU A 180 -178.87 -65.35
REMARK 500 5 GLU A 206 -34.78 -34.41
REMARK 500 5 ASP A 217 73.88 -164.41
REMARK 500 5 ARG A 291 22.17 44.43
REMARK 500 5 PHE A 300 53.43 -115.47
REMARK 500 5 GLN A 303 -68.80 -102.25
REMARK 500 6 ASP A 153 56.66 -95.87
REMARK 500 6 GLU A 206 -35.43 -33.98
REMARK 500 6 ASP A 217 77.26 -169.36
REMARK 500 6 PHE A 235 39.71 -97.21
REMARK 500 6 ARG A 291 26.66 39.75
REMARK 500 6 TRP A 293 -64.12 -29.45
REMARK 500 7 SER A 174 21.02 -144.18
REMARK 500 7 LYS A 175 -119.45 -73.02
REMARK 500 7 GLU A 182 -33.54 -132.26
REMARK 500 7 GLU A 206 -35.42 -34.10
REMARK 500 7 ASP A 217 75.89 -165.46
REMARK 500 7 ARG A 291 25.16 43.64
REMARK 500
REMARK 500 THIS ENTRY HAS 161 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WSX A 152 308 UNP P97287 MCL1_MOUSE 152 308
SEQADV 1WSX GLY A 147 UNP P97287 CLONING ARTIFACT
SEQADV 1WSX PRO A 148 UNP P97287 CLONING ARTIFACT
SEQADV 1WSX LEU A 149 UNP P97287 CLONING ARTIFACT
SEQADV 1WSX GLY A 150 UNP P97287 CLONING ARTIFACT
SEQADV 1WSX SER A 151 UNP P97287 CLONING ARTIFACT
SEQRES 1 A 162 GLY PRO LEU GLY SER GLU ASP ASP LEU TYR ARG GLN SER
SEQRES 2 A 162 LEU GLU ILE ILE SER ARG TYR LEU ARG GLU GLN ALA THR
SEQRES 3 A 162 GLY SER LYS ASP SER LYS PRO LEU GLY GLU ALA GLY ALA
SEQRES 4 A 162 ALA GLY ARG ARG ALA LEU GLU THR LEU ARG ARG VAL GLY
SEQRES 5 A 162 ASP GLY VAL GLN ARG ASN HIS GLU THR ALA PHE GLN GLY
SEQRES 6 A 162 MET LEU ARG LYS LEU ASP ILE LYS ASN GLU GLY ASP VAL
SEQRES 7 A 162 LYS SER PHE SER ARG VAL MET VAL HIS VAL PHE LYS ASP
SEQRES 8 A 162 GLY VAL THR ASN TRP GLY ARG ILE VAL THR LEU ILE SER
SEQRES 9 A 162 PHE GLY ALA PHE VAL ALA LYS HIS LEU LYS SER VAL ASN
SEQRES 10 A 162 GLN GLU SER PHE ILE GLU PRO LEU ALA GLU THR ILE THR
SEQRES 11 A 162 ASP VAL LEU VAL ARG THR LYS ARG ASP TRP LEU VAL LYS
SEQRES 12 A 162 GLN ARG GLY TRP ASP GLY PHE VAL GLU PHE PHE HIS VAL
SEQRES 13 A 162 GLN ASP LEU GLU GLY GLY
HELIX 1 1 ASP A 153 GLY A 173 1 21
HELIX 2 2 GLY A 184 LEU A 216 1 33
HELIX 3 3 ASP A 223 PHE A 235 1 13
HELIX 4 4 ASN A 241 VAL A 262 1 22
HELIX 5 5 GLN A 264 LYS A 283 1 20
HELIX 6 6 LYS A 283 GLN A 290 1 8
HELIX 7 7 GLY A 292 PHE A 300 1 9
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes